Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling (Q44222230)

1 December 2017

Transient structure formation in unfolded acyl-coenzyme A-binding protein observed by site-directed spin labelling (English)

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1 December 2017

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1 December 2017

Flemming M Poulsen

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PubMed ID

12441112

1 December 2017

language of work or name

English

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publication date

1 November 2002

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Journal of Molecular Biology

1 December 2017

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1 December 2017

324

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2

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1 December 2017

349-357

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Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm

1 December 2017

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Understanding protein folding via free-energy surfaces from theory and experiment

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Persistence of native-like topology in a denatured protein in 8 M urea

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Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding

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Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures

7 January 2021

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NMR characterization of residual structure in the denatured state of protein L

7 January 2021

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NOE data demonstrating a compact unfolded state for an SH3 domain under non-denaturing conditions.

7 January 2021

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Long-range interactions within a nonnative protein

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Preorganized secondary structure as an important determinant of fast protein folding

7 January 2021

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Acceleration of the folding of acylphosphatase by stabilization of local secondary structure

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Hydration of denatured and molten globule proteins

7 January 2021

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The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP

7 January 2021

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Formation of hydrogen bonds precedes the rate-limiting formation of persistent structure in the folding of ACBP.

7 January 2021

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The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

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The three-dimensional structure of acyl-coenzyme A binding protein from bovine liver: structural refinement using heteronuclear multidimensional NMR spectroscopy

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Calculation of ensembles of structures representing the unfolded state of an SH3 domain.

7 January 2021

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NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions

7 January 2021

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Mapping the lifetimes of local opening events in a native state protein

7 January 2021

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Fast events in protein folding initiated by nanosecond laser photolysis

7 January 2021

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Two-state expansion and collapse of a polypeptide

7 January 2021

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Chain collapse can occur concomitantly with the rate-limiting step in protein folding

7 January 2021

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Transient intermediary states with high and low folding probabilities in the apparent two-state folding equilibrium of ACBP at low pH.

7 January 2021

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7 January 2021

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The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.

7 January 2021

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Early kinetic intermediate in the folding of acyl-CoA binding protein detected by fluorescence labeling and ultrarapid mixing

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Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition

7 January 2021

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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Automated and semiautomated analysis of homo- and heteronuclear multidimensional nuclear magnetic resonance spectra of proteins: the program Pronto

7 January 2021

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Spin labeling of proteins

7 January 2021

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Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data

7 January 2021

1 reference

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1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

7 January 2021

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Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides.

7 January 2021

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Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence.

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Conformational preferences of amino acids in globular proteins

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A simple method for displaying the hydropathic character of a protein

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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10.1016/S0022-2836(02)01039-2

7 January 2021

Identifiers

DOI

1 reference

1 December 2017

1 reference

PubMed ID

12441112